Glycine Substitution at Helix-to-Coil Transitions Facilitates the Structural Determination of a Stabilized Subtype C HIV Envelope Glycoprotein

Immunity

Volumn 46, Issue 5, 2017, Pages 792-803.e3

  Guenaga, Javier ^a   Garces, Fernando ^a   de Val, Natalia ^a   Stanfield, Robyn L ^a   Dubrovskaya, Viktoriya ^a   Higgins, Brett ^a   Carrette, Barbara ^a   Ward, Andrew B ^a,b   Wilson, Ian A ^a,b   Wyatt, Richard T ^a,b  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery   (United States)

Author keywords

Antibody; bNAb; Envelope glycoprotein; Glycan shield; HIV; Immunogen; Trimer; Vaccine

Indexed keywords

ANTIGEN; CD4 ANTIGEN; ENVELOPE PROTEIN; GLYCINE; GLYCOPROTEIN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; NEUTRALIZING ANTIBODY; PROTEIN BINDING; VIRUS ENVELOPE PROTEIN;

AMINO TERMINAL SEQUENCE; ANTIGEN RECOGNITION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DISULFIDE BOND; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1 INFECTION; HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 SUBTYPE C; IMMUNE EVASION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DETERMINATION; PROTEIN GLYCOSYLATION; PROTEIN STRUCTURE; ALPHA HELIX; AMINO ACID SUBSTITUTION; BINDING SITE; CHEMISTRY; CLASSIFICATION; GENETICS; GENOTYPE; GLYCOSYLATION; HUMAN IMMUNODEFICIENCY VIRUS 1; IMMUNOLOGY; METABOLISM; MOLECULAR MODEL; MUTATION; PROTEIN DEGRADATION; PROTEIN ENGINEERING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; SOLUBILITY; STRUCTURE ACTIVITY RELATION;

AMINO ACID SUBSTITUTION; ANTIBODIES, NEUTRALIZING; BINDING SITES; ENV GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS; GENOTYPE; GLYCINE; GLYCOSYLATION; HIV ANTIBODIES; HIV ENVELOPE PROTEIN GP120; HIV ENVELOPE PROTEIN GP41; HIV-1; HUMANS; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN ENGINEERING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEOLYSIS; SOLUBILITY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 85019482085     PISSN: 10747613     EISSN: 10974180     Source Type: Journal    
DOI: 10.1016/j.immuni.2017.04.014     Document Type: Article

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